ID I8T7F0_9GAMM Unreviewed; 492 AA.
AC I8T7F0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|RuleBase:RU363071};
DE EC=2.5.1.54 {ECO:0000256|RuleBase:RU363071};
GN ORFNames=WQQ_32550 {ECO:0000313|EMBL:EIT69673.1};
OS Hydrocarboniphaga effusa AP103.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Hydrocarboniphaga.
OX NCBI_TaxID=1172194 {ECO:0000313|EMBL:EIT69673.1, ECO:0000313|Proteomes:UP000003704};
RN [1] {ECO:0000313|EMBL:EIT69673.1, ECO:0000313|Proteomes:UP000003704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP103 {ECO:0000313|EMBL:EIT69673.1,
RC ECO:0000313|Proteomes:UP000003704};
RX PubMed=22933753; DOI=10.1128/JB.01017-12;
RA Chang H.K., Zylstra G.J., Chae J.C.;
RT "Genome Sequence of n-Alkane-Degrading Hydrocarboniphaga effusa Strain
RT AP103T (ATCC BAA-332T).";
RL J. Bacteriol. 194:5120-5120(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-
CC phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate;
CC Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54;
CC Evidence={ECO:0000256|RuleBase:RU363071};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR602480-1};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|PIRSR:PIRSR602480-1};
CC Name=Cd(2+); Xref=ChEBI:CHEBI:48775;
CC Evidence={ECO:0000256|PIRSR:PIRSR602480-1};
CC Note=Binds 1 divalent cation per subunit. The enzyme is active with
CC manganese, cobalt or cadmium ions. {ECO:0000256|PIRSR:PIRSR602480-1};
CC -!- SIMILARITY: Belongs to the class-II DAHP synthase family.
CC {ECO:0000256|ARBA:ARBA00008911, ECO:0000256|RuleBase:RU363071}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIT69673.1}.
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DR EMBL; AKGD01000002; EIT69673.1; -; Genomic_DNA.
DR AlphaFoldDB; I8T7F0; -.
DR STRING; 1172194.WQQ_32550; -.
DR PATRIC; fig|1172194.4.peg.3156; -.
DR Proteomes; UP000003704; Unassembled WGS sequence.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002480; DAHP_synth_2.
DR PANTHER; PTHR21337:SF0; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR PANTHER; PTHR21337; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE 1, 2; 1.
DR Pfam; PF01474; DAHP_synth_2; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Cadmium {ECO:0000256|PIRSR:PIRSR602480-1};
KW Cobalt {ECO:0000256|PIRSR:PIRSR602480-1};
KW Manganese {ECO:0000256|PIRSR:PIRSR602480-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003704};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363071}.
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 139
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 176
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 310
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 341
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 373
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 415
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 445
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
SQ SEQUENCE 492 AA; 53331 MW; 583F823445A6EB57 CRC64;
MFNESRLRTG GFRVSRGPSS NELISNDCHR GSGSTPGAKA VFNLDHDVIT GDSIAAADAA
STPRRRSPGS GADAWHPQSW KAHPIRQAPE YPDADAHARV IAQLRQLPPL VLADEVRALK
AQLARVAHGE ALLLQGGDCA ESFAEFSASS LRDTHRTLRE MAIALSTHLP VVTVGRIAGQ
FAKPRSSAAE KIGDVELPSY RGDIVNGPAF DAQSRAPDPQ RMLRAYQQSA ITLNLLRALD
GASIARQSRL YTSHEALLLP YEAASTHRDS VSGDWYDCSA HLLWIGDRTR QLGGAHLEFC
RGIANPLGLK CGPSMTPDEL LRVLDVLDPR REPGRITLIS RMGADGVRDQ LPALVRALQR
EGRPAVWICD PMHGNTQTAT GGYKTRPFER VAEEVRGYFE VHRALGSHAG GLHLEMTGKN
VTECTGGPQQ LSEQDLPLRY QTHCDPRLNA VQALALAAVA RSELASSQAA NTDKARRELP
QSPAETEPLL VT
//
